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Conserved domains on  [gi|2778098843|ref|NP_001419079|]
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coiled-coil domain containing 138 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 189-332 7.20e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 7.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843  189 LLPHQINQIYDELFHIHMKLQNETAAQQKFAEELQKREQFLAEREQLLfrhETALSKIKGVKEEVLTRFQILKEQHSTEI 268
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL---EELNKKIKDLGEEEQLRVKEKIGELEAEI 303

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2778098843  269 EHLTETLKEKNKENKRMRssfDTLRELNDNLRKQLNEVSEENKKMEIQAKR---VQARLDNLQRKYE 332
Cdd:TIGR02169  304 ASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEIEELEREIEEERKRrdkLTEEYAELKEELE 367
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 189-332 7.20e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 7.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843  189 LLPHQINQIYDELFHIHMKLQNETAAQQKFAEELQKREQFLAEREQLLfrhETALSKIKGVKEEVLTRFQILKEQHSTEI 268
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL---EELNKKIKDLGEEEQLRVKEKIGELEAEI 303

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2778098843  269 EHLTETLKEKNKENKRMRssfDTLRELNDNLRKQLNEVSEENKKMEIQAKR---VQARLDNLQRKYE 332
Cdd:TIGR02169  304 ASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEIEELEREIEEERKRrdkLTEEYAELKEELE 367
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 199-337 2.93e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 44.33  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 199 DELFHIHMKLQNETAAQQKFAE-------ELQKREQFLAEREQLLFRH---ETALSKIKGVKEEVLTRFQIL-KEQHSTE 267
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKfknnkevELEELKKILAEDEKLLDEKkqfEKIAEELKGKEQELIFLLQAReKEIHDLE 456

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2778098843 268 IEHLTETLKEKN--KENKRMRSSFDTLRELNDNLRKQLNEVSEENKK-------MEIQAKRVQARLDNLQRKYEFMTVQ 337
Cdd:pfam05483 457 IQLTAIKTSEEHylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEltqeasdMTLELKKHQEDIINCKKQEERMLKQ 535
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
193-339 3.80e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 193 QINQIYDELFHIHMKLQNETAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEVLTRFQILKEQHSTeiehLT 272
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE----LQ 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2778098843 273 ETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYEFMTVQRL 339
Cdd:COG4372   115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 250-312 9.56e-04

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 38.70  E-value: 9.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2778098843 250 KEEVLTRFQILKEQHSTEIEHLTETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKK 312
Cdd:cd22887     9 LEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDE 71
PRK12704 PRK12704
phosphodiesterase; Provisional
 194-325 1.91e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 194 INQIYDELFHIHMKLQNETAAQQKfaeELQKREQFLAEREQLLFRHETALSKikgvKEEVLtrfqilkEQHSTEIEHLTE 273
Cdd:PRK12704   59 LLEAKEEIHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDRKLELLEK----REEEL-------EKKEKELEQKQQ 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2778098843 274 TLKEKNKEnkrmrssfdtLRELNDNLRKQLNEVS----EENKKMEIQAKRVQARLD 325
Cdd:PRK12704  125 ELEKKEEE----------LEELIEEQLQELERISgltaEEAKEILLEKVEEEARHE 170
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 189-332 7.20e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 7.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843  189 LLPHQINQIYDELFHIHMKLQNETAAQQKFAEELQKREQFLAEREQLLfrhETALSKIKGVKEEVLTRFQILKEQHSTEI 268
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL---EELNKKIKDLGEEEQLRVKEKIGELEAEI 303

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2778098843  269 EHLTETLKEKNKENKRMRssfDTLRELNDNLRKQLNEVSEENKKMEIQAKR---VQARLDNLQRKYE 332
Cdd:TIGR02169  304 ASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEIEELEREIEEERKRrdkLTEEYAELKEELE 367
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 193-338 9.55e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 9.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843  193 QINQIYDELFHI---HMKLQNETAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEVLTRFQILKEQHSTEIE 269
Cdd:TIGR02168  790 QIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2778098843  270 HLTETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYEFMTVQR 338
Cdd:TIGR02168  870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 199-337 2.93e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 44.33  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 199 DELFHIHMKLQNETAAQQKFAE-------ELQKREQFLAEREQLLFRH---ETALSKIKGVKEEVLTRFQIL-KEQHSTE 267
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKfknnkevELEELKKILAEDEKLLDEKkqfEKIAEELKGKEQELIFLLQAReKEIHDLE 456

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2778098843 268 IEHLTETLKEKN--KENKRMRSSFDTLRELNDNLRKQLNEVSEENKK-------MEIQAKRVQARLDNLQRKYEFMTVQ 337
Cdd:pfam05483 457 IQLTAIKTSEEHylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEltqeasdMTLELKKHQEDIINCKKQEERMLKQ 535
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
193-339 3.80e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 193 QINQIYDELFHIHMKLQNETAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEVLTRFQILKEQHSTeiehLT 272
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE----LQ 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2778098843 273 ETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYEFMTVQRL 339
Cdd:COG4372   115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 193-332 5.56e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 5.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843  193 QINQIYDELfhIHMKLQNETAAQQKFAEELQKREQFLAEREQ----LLFRHETALSKIKGVKEEVL----TRFQILKEQH 264
Cdd:TIGR02169  780 ALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQklnrLTLEKEYLEKEIQELQEQRIdlkeQIKSIEKEIE 857

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843  265 S--TEIEHLTETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYE 332
Cdd:TIGR02169  858 NlnGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
212-332 6.41e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 6.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 212 TAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEvLTRFQILKEQHSTEIEHLTETLKEKNKENKRMRSSFDT 291
Cdd:COG4372    27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE-LEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2778098843 292 LRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYE 332
Cdd:COG4372   106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA 146
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 212-329 8.37e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 8.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843  212 TAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEVLTRfqiLKEQHSTEIEHLTETLKEKNKENKRMRSSFDT 291
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL---LKKLEEAELKELQAELEELEEELEELQEELER 458

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2778098843  292 LRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQR 329
Cdd:TIGR02168  459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 250-312 9.56e-04

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 38.70  E-value: 9.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2778098843 250 KEEVLTRFQILKEQHSTEIEHLTETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKK 312
Cdd:cd22887     9 LEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDE 71
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
185-330 1.44e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 185 KKQGLLPHQINQIYDELFHIHMKLQNE---TAAQQKFAEELQKREQFLAEREQLLFRHE---TALSKIKGVKEEVLTRFQ 258
Cdd:COG1340   102 AELNKAGGSIDKLRKEIERLEWRQQTEvlsPEEEKELVEKIKELEKELEKAKKALEKNEklkELRAELKELRKEAEEIHK 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2778098843 259 ILKE------QHSTEIEHLTETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRK 330
Cdd:COG1340   182 KIKElaeeaqELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKRE 259
PRK12704 PRK12704
phosphodiesterase; Provisional
 194-325 1.91e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 194 INQIYDELFHIHMKLQNETAAQQKfaeELQKREQFLAEREQLLFRHETALSKikgvKEEVLtrfqilkEQHSTEIEHLTE 273
Cdd:PRK12704   59 LLEAKEEIHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDRKLELLEK----REEEL-------EKKEKELEQKQQ 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2778098843 274 TLKEKNKEnkrmrssfdtLRELNDNLRKQLNEVS----EENKKMEIQAKRVQARLD 325
Cdd:PRK12704  125 ELEKKEEE----------LEELIEEQLQELERISgltaEEAKEILLEKVEEEARHE 170
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 185-334 2.55e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 185 KKQGLLPHQINQIYDELFHIHMKLQNETAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKE-EVLTR-FQILKE 262
Cdd:COG1579    24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyEALQKeIESLKR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 263 QHST----------EIEHLTETLKEKNKENKRMRSSFDTLRElndNLRKQLNEVSEENKKMEIQAKRVQARLD-NLQRKY 331
Cdd:COG1579   104 RISDledeilelmeRIEELEEELAELEAELAELEAELEEKKA---ELDEELAELEAELEELEAEREELAAKIPpELLALY 180


                  ...
gi 2778098843 332 EFM 334
Cdd:COG1579   181 ERI 183
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 215-370 2.90e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.65  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 215 QQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEVLTRFQILKEQHSTEIEHLTEtLKEKNKENKRMRSS----FD 290
Cdd:pfam07888  40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEE-LEEKYKELSASSEElseeKD 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 291 TLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYEFMTVQRlkGDSHAAHE-----VKSSKQEKVPASKPFKA 365
Cdd:pfam07888 119 ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR--KEEEAERKqlqakLQQTEEELRSLSKEFQE 196


                  ....*
gi 2778098843 366 ALNGQ 370
Cdd:pfam07888 197 LRNSL 201
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
192-332 4.74e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 192 HQINQIYDELfhihMKLQNETAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEVLTRFQILKEqhstEIEHL 271
Cdd:PRK03918  207 REINEISSEL----PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK----EIEEL 278

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2778098843 272 TETLKEKnKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYE 332
Cdd:PRK03918  279 EEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 193-366 7.60e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 7.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 193 QINQIYDELFHIHMKLQNETAAQQKFAEELQKREQFLAEREQLLFRHETA-----LSKIKGVKEEV--LTRFQILKEQHS 265
Cdd:COG4942    70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalLLSPEDFLDAVrrLQYLKYLAPARR 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 266 TEIEHLTETLKEKNKENKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYEFMT--VQRLKgDS 343
Cdd:COG4942   150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQqeAEELE-AL 228

                         170       180
                  ....*....|....*....|...
gi 2778098843 344 HAAHEVKSSKQEKVPASKPFKAA 366
Cdd:COG4942   229 IARLEAEAAAAAERTPAAGFAAL 251
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 207-332 9.43e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.37  E-value: 9.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 207 KLQNETAAQQKFAEELQKREQFLAEREQLLFRHETALSKIKGVKEEV---LTRFQILKEQHSTEIEHLTETLKE--KNKE 281
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLekeIKRLELEIEEVEARIKKYEEQLGNvrNNKE 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2778098843 282 NKRMRSSFDTLRELNDNLRKQLNEVSEENKKMEIQAKRVQARLDNLQRKYE 332
Cdd:COG1579    91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
220-374 9.70e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 9.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098843 220 EELQKREQFLAEREQLLFRHETaLSKIKGVKEEVLTRFQILKEQHSTEIEHLTETLKEKNKENKRMRSsfdtLRELNDNL 299
Cdd:PRK03918  276 EELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKEL 350

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2778098843 300 RKQLNEVSEENKKMEiQAKRVQARLDNLQRKYEFMTVQRLKGDSHAAHEVKSSKQEKVPASKPFKAALNGQVYEL 374
Cdd:PRK03918  351 EKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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